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Anti-serum

Davenport, T.R.B., Lee, D.L. and Isaac, R.E. (1988) Immunocytochemical demonstration of a neuropeptide in Ascaris suum (Nematoda) using an anti-serum to FMRFamide. Parasitology 97, 81-88. [Pg.445]

Ziegler, E. J., McCutchan, J. A., Fierer, J. et al. (1982). Treatment of gram-negative bacteremia and shock with human anti-serum to a mutant Escherichia coli. N. Eng. J. Med. 307,1225-1230. [Pg.408]

Fhe antiserum concentration used in the gel may be varied widely. It is determined empirically against an antigen dilution series. To begin rith, 1% anti.serum (v/v) in the gel is advisable. [Pg.203]

The ELISA technique is used for detection of antibodies in serum bound to BPDE-DNA adducts. The USERIA method involves measuring the immunological response of BPDE-DNA in the presence of rabbit anti-serum. Several researchers have employed the immunoassay techniques for detecting PAH-DNA adducts at 10 mol levels in the blood and tissues of humans occupationally exposed to PAHs (Harris et al. 1985 Haugen et al. 1986 Newman et al. 1988 Perera et al. 1988 Shamsuddin et al. 1985 Weston et al. 1988). [Pg.326]

Cohen, S. (1960) Purification of a nerve growth promoting protein from the mouse salivary gland and its neurocyto-toxic anti-serum. Proc. Natl. Acad. Sci. USA 46 302-311. [Pg.193]

Finally, profilins have been reported as residents of the nucleus. Immunofluorescence revealed nuclear profilin I in fibroblasts and epithehal cells (Mayboroda et al. 1997 Skare et al. 2003) and in bovine oocyte germinal vesicles and early embryos (Rawe et al. 2006). Nuclear profilin has also been described in several higher plants (see Hussey et al. 2006 for original references). Additionally, the existence of nuclear profilin-actin complexes can be deduced from studies on HeLa cells and Xenopus oocytes (Striven et al. 2003). In a recent study with GFP-profilin transfected cells and polyclonal anti-serum, profilin II has been shown to accumulate in the nucleus of hippocampal neurons. This concentration was de-... [Pg.138]

AntUAB Anil species anti serum against species from donor AB... [Pg.12]

This chapter describes the production of anti-serums, the purification of antibodies, and the most important immunological screening technologies. For monoclonal antibodies, I refer you to Methods Enzymol. I (1986) 121, Hybridoma Technology and Monoclonal Antibodies. I also touch only briefly upon the newer in-vitro immunization methods in the following (with friendly consultation from Dr. Rose-John, Mainz). [Pg.137]

It therefore results from all this data that plasteins arc of a very complex protein nature, which approache.s in certain points that of natural albuminoids, but which differs from it, however, from the point of view of formaldehyde nitrogen. The special nature of plasteins and their differentiation from the natural albumins appears also from the work of Herrmann and Chain. By inoculation of rabbits with plastein coming from Witte peptone, consequently from fibrin, they obtained an anti-serum which... [Pg.287]

Primary antibodies or anti-serum, for example, rabbit anti-serum. [Pg.179]

Two lipases, i.e. LPL and H-TGL, in this postheparin plasma were separately measured using the antiserum prepared against H-TGL(3). Plasma samples from 12 age-matched control subjects were used for the lipoprotein analysis. Normal values of postheparin plasma lipase activities were those for 13 normo-lipidemic male subjects reported elesewhere(3). The serum concentration of apolipoprotein A-I, A-IE and apolipoprotein B were measured by a immunodiffusion technique using specific anti-serum. [Pg.137]

Anti-03-D-2-acetamido-2-deoxyglucosidase) antibody Anti-(serum albumin) antibody... [Pg.517]

Clements-Jewery H, Hearse DJ, Curtis MJ (2007) Neutrophil ablation with anti-serum does not protect against phase 2 ventricular arrhythmias in anaesthetised rats with myocardial infarction. Cardiovasc Res 73 761-769... [Pg.198]

In the experiment shown in Figure 4.13, three different concentrations of AEF were directly absorbed independently by immunoadsorbents prepared from (B6A)Fi anti-B10.D2 and BIO.A anti-BlO alloantisera and by an adsorbent prepared from normal BIO.A serum. These AEF were then compared to unabsorbed AEF for biological activity on the in vitro response to SRBC of DBA/2 B lymphocytes. As shown in Figure 4.13, cultures of untreated control whole spleen cells developed primary IgG anti-SRBC responses of around 1200 PFC anti-0 treatment diminished this response to around 150 PFC. The addition of unabsorbed AEF to such anti-0 serum-treated B cells reconstituted and enriched the response markedly and in a dose-related manner at all three concentrations of AEF employed. The AEF subjected to the adsorbent prepared from (B6A)Fj anti-B10.D2 serum retained essentially normal biological activity at the highest concentration (1 5), but the lowest concentration subjected to absorption (1 20) was around 45% lower in activity than the normal serum control. The AEF subjected to the BIO.A anti-BlO (anti-la) im-munoadsorbent, on the other hand, exhibited markedly diminished (80% or more) activity at all three concentrations indicating substantial reactivity of this anti-serum with the biologically active component(s) of AEF . ... [Pg.168]

The fruit of Thaumatococcus daniellii contains two sweet proteins thaumatin I and II, with /sac,g 2000. There are also low amounts of three other sweet proteins (thaumatin a, b and c). The complete amino acid sequence and the conformation (Fig. 8.7 and 8.8) of thaumatin I, a peptide chain with 207 amino acid residues, has been established (Table 8.5). As a result of cross reactions with an anti-serum against monellin (cf. 8.8.4), sequence Y(57)FD in a j3-tum is regarded as the site of contact with the sweetness receptor. It corresponds to sequence Y(A13)ASD of monellin. [Pg.437]

A. Koide, S. Kobayashi, Modification of amino groups in porcine pancreatic elastase with polyethylene glycol in relation to binding ability towards anti-serum and to enzymic activity. Biochem. Bioph. Res. Go., Ill (2) 659-667,1983. [Pg.91]

A. Matsushima, H. Nishimura, Y. Ashihara, Modification of E. coli asparaginase with 2,4-bis(0-methoxypolyethylene glycol)-6-chloro-S-triazine (activated PEG2) disappearance of binding ability towards anti-serum and retention of enzymatic activity. Ghem. Lett, 9 (7) 773-776,1980. [Pg.91]


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See also in sourсe #XX -- [ Pg.686 ]




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